- Home
- 42 b
- Endocytic uptake of monomeric amyloid-β peptides is clathrin- and dynamin-independent and results in selective accumulation of Aβ(1–42) compared to Aβ(1–40)
Endocytic uptake of monomeric amyloid-β peptides is clathrin- and dynamin-independent and results in selective accumulation of Aβ(1–42) compared to Aβ(1–40)
4.6 (675) · $ 17.00 · In stock
Cell surface proteoglycan-mediated uptake and accumulation of the Alzheimer's disease peptide Aβ(1–42) - ScienceDirect
The amyloid-β degradation intermediate Aβ34 is pericyte-associated and reduced in brain capillaries of patients with Alzheimer's disease, Acta Neuropathologica Communications
IJMS, Free Full-Text
Frontiers Amyloid Beta Is Internalized via Macropinocytosis, an HSPG- and Lipid Raft-Dependent and Rac1-Mediated Process
Misfolded amyloid-β-42 impairs the endosomal–lysosomal pathway
The amyloid-β degradation intermediate Aβ34 is pericyte-associated and reduced in brain capillaries of patients with Alzheimer's disease, Acta Neuropathologica Communications
Endocytic uptake of monomeric amyloid-β peptides is clathrin- and dynamin- independent and results in selective accumulation of Aβ(1–42) compared to Aβ (1–40)
In vivo synaptic activity-independent co-uptakes of amyloid β1–42 and Zn2+ into dentate granule cells in the normal brain
Contribution of syndecans to cellular internalization and fibrillation of amyloid-β(1–42)
IJMS, Free Full-Text
IJMS, Free Full-Text
Frontiers Amyloid Beta Is Internalized via Macropinocytosis, an HSPG- and Lipid Raft-Dependent and Rac1-Mediated Process
